ID A0A1J1HUZ8_9DIPT Unreviewed; 722 AA.
AC A0A1J1HUZ8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
GN ORFNames=CLUMA_CG005450 {ECO:0000313|EMBL:CRK91827.1};
OS Clunio marinus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Clunio.
OX NCBI_TaxID=568069 {ECO:0000313|EMBL:CRK91827.1, ECO:0000313|Proteomes:UP000183832};
RN [1] {ECO:0000313|EMBL:CRK91827.1, ECO:0000313|Proteomes:UP000183832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001171,
CC ECO:0000256|RuleBase:RU000312};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily.
CC {ECO:0000256|RuleBase:RU000312}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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DR EMBL; CVRI01000021; CRK91827.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J1HUZ8; -.
DR Proteomes; UP000183832; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR CDD; cd00108; KR; 1.
DR CDD; cd05048; PTKc_Ror; 1.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 2.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR PANTHER; PTHR24416:SF611; TYROSINE-PROTEIN KINASE TRANSMEMBRANE RECEPTOR ROR; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 3.
DR PRINTS; PR00018; KRINGLE.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00130; KR; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Phosphoprotein {ECO:0000256|RuleBase:RU000312};
KW Receptor {ECO:0000256|RuleBase:RU000312};
KW Reference proteome {ECO:0000313|Proteomes:UP000183832};
KW Transmembrane {ECO:0000256|RuleBase:RU000312, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 332..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..246
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 257..328
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 425..689
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 699..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 554
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 457
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 559
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 572
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT DISULFID 300..323
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 722 AA; 82998 MW; B99DF8FAD0436F2E CRC64;
MGICQPYTGK ICERWMRNQT VFISPETTMD MLEEKLARAY GVIKESKDMN TICSKFAVPS
LCITVLPICR TPEESNHYFF LNKNKAKSVD KFITKKAKKS NKKKTTTPRS LVFKSAFALT
TASTTTTTIS STSSTTKKPE KYDHVEFSSN SNSYYEPSSY HATDHPFNHL RKRRNVDVDF
LSIRNAYPPT KHSENLRRIC RADCELLENE ICQKEYAIAK RHPTIGQILP LEDCNEVPDD
DDCLRMGINV DINPSDTCFW DNGNQYRGIK DKSINGKPCL KWSKVLREIT HIELANNNYC
RNPDASQSKP WCYVDKQKTV ELCDIPKCSD KMWFVIICAL ILFLMTTMFI TILVCCKKMR
RQSVSNIQNI TVPNVDKNIY GNSRHSSPIE MTSLLATNGM SNLHHPTNPR GNSIMKIPQY
GLQDVKFVEE LGEGAFGKVY KGELFQKNGE KTFVAVKALK ENASPKTQQD FRREIELISD
LKHTNIVCIL GVVLKEEPLC MLFEYMSHGD LHEYLISNSP NEGKYLSQQQ FLFISLQIAE
GMEYLSNHHY VHRDLAARNC LVGDDMIVKI SDFGLSRDIY SSDYYRVQSK SLLPVRWMPS
EAILYGKFTT ESDVWSYGVV LWEIYSYGIQ PYFGYSNQEV INMVRARQLL ACPEACPSAV
YSLMVECWHE QSVRRPNFAE IVHRLRVWYQ SQRRRDQMEI NTGSMNRQPS TTGSTISVRS
FK
//
